Person:
Alcolea Palafox, Mauricio

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First Name
Mauricio
Last Name
Alcolea Palafox
URI
https://hdl.handle.net/20.500.14352/76202
Affiliation
Universidad Complutense de Madrid
Faculty / Institute
Ciencias Químicas
Department
Química Física
Area
Química Física
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Author: Akitsu, Takashiro × End date: 2019 ×

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    Investigation by DFT Methods of the Damage of Human Serum Albumin Including Amino Acid Derivative Schiff Base Zn(II) Complexes by IR-FEL Irradiation
    (International Journal of Molecular Sciences, 2019) Onami, Yuika; Koya, Ryousuke; Kawasaki, Takayasu; Aizawa, Hiroki; Nakagame, Ryo; Miyagawa, Yoshito; Haraguchi, Tomoyuki; Akitsu, Takashiro; Tsukiyama, Koichi; Alcolea Palafox, Mauricio
    An infrared free electron laser (IR-FEL) can decompose aggregated proteins by excitation of vibrational bands. In this study, we prepared hybrid materials of protein (human serum albumin; HSA) including several new Schiff base Zn(II) complexes incorporating amino acid (alanine and valine) or dipeptide (gly-gly) derivative moieties, which were synthesized and characterized with UV-vis, circular dichroism (CD), and IR spectra. Density functional theory (DFT) and time dependent DFT (TD-DFT) calculations were also performed to investigate vibrational modes of the Zn(II) complexes. An IR-FEL was used to irradiate HSA as well as hybrid materials of HSA-Zn(II) complexes at wavelengths corresponding to imine C=N, amide I, and amide II bands. Analysis of secondary structures suggested that including a Zn(II) complex into HSA led to the structural change of HSA, resulting in a more fragile structure than the original HSA. The result was one of the characteristic features of vibrational excitation of IR-FEL in contrast to electronic excitation by UV or visible light.